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P00909

- TRPC_ECOLI

UniProt

P00909 - TRPC_ECOLI

Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (19 Mar 2014)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain.

    Catalytic activityi

    N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
    1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

    Pathwayi

    GO - Molecular functioni

    1. indole-3-glycerol-phosphate synthase activity Source: EcoCyc
    2. phosphoribosylanthranilate isomerase activity Source: EcoCyc

    GO - Biological processi

    1. tryptophan biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Decarboxylase, Isomerase, Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:PRAI-IGPS.
    ECOL316407:JW1254-MONOMER.
    MetaCyc:PRAI-IGPS.
    UniPathwayiUPA00035; UER00042.
    UPA00035; UER00043.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan biosynthesis protein TrpCF
    Including the following 2 domains:
    Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
    Short name:
    IGPS
    N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
    Short name:
    PRAI
    Gene namesi
    Name:trpC
    Synonyms:trpF
    Ordered Locus Names:b1262, JW1254
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11026. trpC.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Tryptophan biosynthesis protein TrpCFPRO_0000154277Add
    BLAST

    Proteomic databases

    PaxDbiP00909.
    PRIDEiP00909.

    Expressioni

    Gene expression databases

    GenevestigatoriP00909.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiP00909. 7 interactions.
    STRINGi511145.b1262.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2319
    Helixi26 – 283
    Helixi30 – 323
    Helixi40 – 445
    Beta strandi46 – 483
    Beta strandi50 – 556
    Beta strandi57 – 593
    Turni60 – 623
    Beta strandi63 – 653
    Helixi71 – 788
    Turni79 – 813
    Beta strandi83 – 886
    Turni92 – 943
    Helixi100 – 1078
    Beta strandi112 – 1165
    Helixi121 – 1299
    Beta strandi133 – 1386
    Turni139 – 1413
    Helixi144 – 15613
    Beta strandi160 – 1656
    Helixi168 – 1769
    Beta strandi180 – 1878
    Turni189 – 1913
    Helixi197 – 20610
    Beta strandi210 – 2167
    Helixi221 – 2277
    Turni228 – 2303
    Beta strandi232 – 2365
    Helixi238 – 2414
    Helixi246 – 25510
    Helixi266 – 27510
    Beta strandi278 – 2836
    Helixi294 – 30310
    Beta strandi307 – 3148
    Helixi317 – 32711
    Beta strandi330 – 3345
    Helixi336 – 3383
    Helixi340 – 34910
    Beta strandi354 – 3618
    Beta strandi363 – 3653
    Beta strandi376 – 3816
    Helixi392 – 3954
    Beta strandi403 – 4086
    Turni411 – 4133
    Helixi414 – 4185
    Beta strandi423 – 4275
    Helixi429 – 4313
    Beta strandi432 – 4343
    Helixi440 – 45112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCMX-ray2.10P2-260[»]
    1PIIX-ray2.00A2-453[»]
    2KZHNMR-A256-385[»]
    ProteinModelPortaliP00909.
    SMRiP00909. Positions 2-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00909.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 257257Indole-3-glycerol phosphate synthaseAdd
    BLAST
    Regioni258 – 453196N-(5'-phosphoribosyl)anthranilate isomeraseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the TrpC family.Curated
    In the C-terminal section; belongs to the TrpF family.Curated

    Phylogenomic databases

    eggNOGiCOG0134.
    HOGENOMiHOG000280458.
    KOiK13498.
    OMAiEKYFQGD.
    OrthoDBiEOG6WT8JX.

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    HAMAPiMF_00134_B. IGPS_B.
    MF_00135. PRAI.
    InterProiIPR013785. Aldolase_TIM.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 2 hits.
    PROSITEiPS00614. IGPS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00909-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA    50
    FILECKKASP SKGVIRDDFD PARIAAIYKH YASAISVLTD EKYFQGSFNF 100
    LPIVSQIAPQ PILCKDFIID PYQIYLARYY QADACLLMLS VLDDDQYRQL 150
    AAVAHSLEMG VLTEVSNEEE QERAIALGAK VVGINNRDLR DLSIDLNRTR 200
    ELAPKLGHNV TVISESGINT YAQVRELSHF ANGFLIGSAL MAHDDLHAAV 250
    RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV 300
    MAAAPLQYVG VFRNHDIADV VDKAKVLSLA AVQLHGNEEQ LYIDTLREAL 350
    PAHVAIWKAL SVGETLPARE FQHVDKYVLD NGQGGSGQRF DWSLLNGQSL 400
    GNVLLAGGLG ADNCVEAAQT GCAGLDFNSA VESQPGIKDA RLLASVFQTL 450
    RAY 453
    Length:453
    Mass (Da):49,492
    Last modified:March 19, 2014 - v4
    Checksum:i09D5DA2353291F33
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311Missing in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti95 – 951Q → R in CAA23664. (PubMed:7007653)Curated
    Sequence conflicti95 – 951Q → R in AAA57299. (PubMed:7007653)Curated
    Sequence conflicti95 – 951Q → R in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti285 – 2851Missing in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti294 – 2941V → D in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti330 – 3301A → V in CAA23664. (PubMed:7007653)Curated
    Sequence conflicti330 – 3301A → V in AAA57299. (PubMed:7007653)Curated
    Sequence conflicti330 – 3301A → V in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti399 – 3991S → T in CAA23664. (PubMed:7007653)Curated
    Sequence conflicti399 – 3991S → T in AAA57299. (PubMed:7007653)Curated
    Sequence conflicti399 – 3991S → T in CAA23673. (PubMed:7038627)Curated
    Sequence conflicti399 – 3991S → T in AAB60033. (PubMed:8095913)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00366 Genomic DNA. Translation: CAA23664.1.
    V00372 Genomic DNA. Translation: CAA23673.1.
    J01714 Genomic DNA. Translation: AAA57299.1.
    U23489 Genomic DNA. Translation: AAB60033.1.
    U00096 Genomic DNA. Translation: AAC74344.3.
    AP009048 Genomic DNA. Translation: BAA14794.1.
    PIRiA64874. GWEC.
    RefSeqiNP_415778.3. NC_000913.3.
    YP_489530.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74344; AAC74344; b1262.
    BAA14794; BAA14794; BAA14794.
    GeneIDi12931128.
    945519.
    KEGGiecj:Y75_p1236.
    PATRICi32117784. VBIEscCol129921_1312.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00366 Genomic DNA. Translation: CAA23664.1 .
    V00372 Genomic DNA. Translation: CAA23673.1 .
    J01714 Genomic DNA. Translation: AAA57299.1 .
    U23489 Genomic DNA. Translation: AAB60033.1 .
    U00096 Genomic DNA. Translation: AAC74344.3 .
    AP009048 Genomic DNA. Translation: BAA14794.1 .
    PIRi A64874. GWEC.
    RefSeqi NP_415778.3. NC_000913.3.
    YP_489530.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JCM X-ray 2.10 P 2-260 [» ]
    1PII X-ray 2.00 A 2-453 [» ]
    2KZH NMR - A 256-385 [» ]
    ProteinModelPortali P00909.
    SMRi P00909. Positions 2-453.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00909. 7 interactions.
    STRINGi 511145.b1262.

    Proteomic databases

    PaxDbi P00909.
    PRIDEi P00909.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74344 ; AAC74344 ; b1262 .
    BAA14794 ; BAA14794 ; BAA14794 .
    GeneIDi 12931128.
    945519.
    KEGGi ecj:Y75_p1236.
    PATRICi 32117784. VBIEscCol129921_1312.

    Organism-specific databases

    EchoBASEi EB1019.
    EcoGenei EG11026. trpC.

    Phylogenomic databases

    eggNOGi COG0134.
    HOGENOMi HOG000280458.
    KOi K13498.
    OMAi EKYFQGD.
    OrthoDBi EOG6WT8JX.

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00042 .
    UPA00035 ; UER00043 .
    BioCyci EcoCyc:PRAI-IGPS.
    ECOL316407:JW1254-MONOMER.
    MetaCyc:PRAI-IGPS.

    Miscellaneous databases

    EvolutionaryTracei P00909.
    PROi P00909.

    Gene expression databases

    Genevestigatori P00909.

    Family and domain databases

    Gene3Di 3.20.20.70. 2 hits.
    HAMAPi MF_00134_B. IGPS_B.
    MF_00135. PRAI.
    InterProi IPR013785. Aldolase_TIM.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 2 hits.
    PROSITEi PS00614. IGPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions."
      Christie G.E., Platt T.
      J. Mol. Biol. 142:519-530(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium."
      Horowitz H., van Arsdell J., Platt T.
      J. Mol. Biol. 169:775-797(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 95 AND 399.
    3. "The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
      Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
      Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons."
      Milkman R., Bridges M.M.
      Genetics 133:455-468(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments."
      Krug K., Carpy A., Behrends G., Matic K., Soares N.C., Macek B.
      Mol. Cell. Proteomics 12:3420-3430(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-8.
      Strain: K12 / BW25113.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0-A resolution."
      Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N.
      J. Mol. Biol. 223:477-507(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 320.
    11. "Crystallization and structure solution at 4-A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue."
      Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N.
      Protein Eng. 3:173-180(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 258-453.

    Entry informationi

    Entry nameiTRPC_ECOLI
    AccessioniPrimary (citable) accession number: P00909
    Secondary accession number(s): P78059, P78234, P94704
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 19, 2014
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3